ID Card:
Full name:
Methylenetetrahydrofolate--tRNA-(uracil-54-)-methyltransferase TrmFO
Synonym:
Gid, YlyC
GI:
3183519
Orf:
BSU16130
COG:
COG1206
UniProt:
P39815
Alpha Fold Predicted Structure:
AF-P39815-F1
Enzyme type:
methyltransferase
Position of modification - modification:
t :54 - m5U
Protein sequence:
MNQQTVNVIGAGLAGSEAAWQLAKRGIQVKLYEMRPVKQTPAHHTDKFAELVCSNSLRSNTLANAVGVLKEEMRALDSAIIAAADECSVPAGGALAVDRHEFAASVTNRVKNHPNVTVINEEVTEIPEGPTIIATGPLTSESLSAQLKELTGEDYLYFYDAAAPIVEKDSLDMDKVYLKSRYDKGEAAYLNCPMTEEEFDRFHEALTSAETVPLKEFEKEIFFEGCMPIEVMAKRGKKTMLFGPMKPVGLEHPVTGKRPYAVVQLRQDDAAGTLYNIVGFQTHLKWGDQKEVLKLIPGLENVEIVRYGVMHRNTFINSPSLLKPTYQFKNRSDLFFAGQMTGVEGYVESAASGLVAGINAAKLVLGEELVIFPQETAIGSMAHYITTTNQKNFQPMNANFGLLKELPVKIKNKKERNEQYANRAIETIQTISKTI
Comments:
In all Eukarya and many Gram-negative Bacteria, the methyl donor for this reaction is S-adenosyl-L-methionine (S-AdoMet), while in several Gram-positive Bacteria, the source of carbon is N5, N10-methylenetetrahydrofolate (CH2H4folate) . Modification in position 54 has been mapped in all tRNAs(
Urbonavičius et al. 2005 ). Enzymatic reactions has been mapped to the MODOMICS RNA dataset. Therefore, more tRNA isoacepptors could be available.
Alpha Fold Predicted Structure:
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Protein sequence:
M
N
Q
Q
T
V
N
V
I
G
A
G
L
A
G
S
E
A
A
W
Q
L
A
K
R
G
I
Q
V
K
L
Y
E
M
R
P
V
K
Q
T
P
A
H
H
T
D
K
F
A
E
L
V
C
S
N
S
L
R
S
N
T
L
A
N
A
V
G
V
L
K
E
E
M
R
A
L
D
S
A
I
I
A
A
A
D
E
C
S
V
P
A
G
G
A
L
A
V
D
R
H
E
F
A
A
S
V
T
N
R
V
K
N
H
P
N
V
T
V
I
N
E
E
V
T
E
I
P
E
G
P
T
I
I
A
T
G
P
L
T
S
E
S
L
S
A
Q
L
K
E
L
T
G
E
D
Y
L
Y
F
Y
D
A
A
A
P
I
V
E
K
D
S
L
D
M
D
K
V
Y
L
K
S
R
Y
D
K
G
E
A
A
Y
L
N
C
P
M
T
E
E
E
F
D
R
F
H
E
A
L
T
S
A
E
T
V
P
L
K
E
F
E
K
E
I
F
F
E
G
C
M
P
I
E
V
M
A
K
R
G
K
K
T
M
L
F
G
P
M
K
P
V
G
L
E
H
P
V
T
G
K
R
P
Y
A
V
V
Q
L
R
Q
D
D
A
A
G
T
L
Y
N
I
V
G
F
Q
T
H
L
K
W
G
D
Q
K
E
V
L
K
L
I
P
G
L
E
N
V
E
I
V
R
Y
G
V
M
H
R
N
T
F
I
N
S
P
S
L
L
K
P
T
Y
Q
F
K
N
R
S
D
L
F
F
A
G
Q
M
T
G
V
E
G
Y
V
E
S
A
A
S
G
L
V
A
G
I
N
A
A
K
L
V
L
G
E
E
L
V
I
F
P
Q
E
T
A
I
G
S
M
A
H
Y
I
T
T
T
N
Q
K
N
F
Q
P
M
N
A
N
F
G
L
L
K
E
L
P
V
K
I
K
N
K
K
E
R
N
E
Q
Y
A
N
R
A
I
E
T
I
Q
T
I
S
K
T
I
50 100 150 200 250 300 350 400 Sequence G H T B S N
Secondary Structure Alphabet
G: 3-turn helix (310 helix)
H: α-helix
I: 𝝅-helix (5 - turn helix)
T: Hydrogen Bonded Turn
B: β-sheet
S: Bend
C: Coil (residues not present in any of the above conformations)
N: Not assigned
Download PDB Structures & DSSP Secondary Structures:
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